Interaction of 14-3-3 proteins with their targets depends not only on the phosphorylation status of the target but also on that of 14-3-3 (Fu et al., 2000). In this work we demonstrated that the maize 14-3-3 isoform GF14-6 is a substrate of the tyrosine kinase insulin growth factor receptor 1. By means of site-directed mutants of GF14-6, we identified Tyr-137 as the specific tyrosine residue phosphorylated by the insulin growth factor receptor 1. Phosphorylation of GF14-6 on Tyr-137 lowered its affinity for a peptide mimicking the 14-3-3 binding site of the plant plasma membrane H+-ATPase. Moreover, phosphorylation in planta of 14-3-3 tyrosine residues, resulting from incubation with the tyrosine phosphatase inhibitor, phenylarsine oxide, decreased their association to the H+-ATPase.
Titolo: | Tyrosine phosphorylation inhibits the interaction of 14-3-3 proteins with the plant plasma membrane H+-ATPase |
Autori: | GIACOMETTI, SONIA (Primo) DE MICHELIS, MARIA IDA (Penultimo) |
Parole Chiave: | 14-3-3 proteins; Plasma membrane H+-ATPase; Signal transduction; Tyrosine phosphorylation |
Settore Scientifico Disciplinare: | Settore BIO/04 - Fisiologia Vegetale |
Data di pubblicazione: | 2004 |
Rivista: | |
Tipologia: | Article (author) |
Digital Object Identifier (DOI): | 10.1055/s-2004-820933 |
Appare nelle tipologie: | 01 - Articolo su periodico |